ID   S36A2_MOUSE             Reviewed;         478 AA.
AC   Q8BHK3; Q8BUB0; Q8JZP1;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Proton-coupled amino acid transporter 2 {ECO:0000305|PubMed:11959859};
DE            Short=Proton/amino acid transporter 2 {ECO:0000303|PubMed:11959859};
DE   AltName: Full=Solute carrier family 36 member 2 {ECO:0000312|MGI:MGI:1891430};
DE   AltName: Full=Transmembrane domain rich protein 1 {ECO:0000303|PubMed:12451123};
DE            Short=Tramdorin-1 {ECO:0000303|PubMed:12451123};
GN   Name=Slc36a2 {ECO:0000312|MGI:MGI:1891430};
GN   Synonyms=Pat2 {ECO:0000303|PubMed:11959859}, Tramd1
GN   {ECO:0000303|PubMed:12451123};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC   STRAIN=C57BL/6J;
RX   PubMed=11959859; DOI=10.1074/jbc.m200374200;
RA   Boll M., Foltz M., Rubio-Aliaga I., Kottra G., Daniel H.;
RT   "Functional characterization of two novel mammalian electrogenic proton-
RT   dependent amino acid cotransporters.";
RL   J. Biol. Chem. 277:22966-22973(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   PubMed=12451123; DOI=10.1523/jneurosci.22-23-10217.2002;
RA   Bermingham J.R. Jr., Shumas S., Whisenhunt T., Sirkowski E.E.,
RA   O'Connell S., Scherer S.S., Rosenfeld M.G.;
RT   "Identification of genes that are downregulated in the absence of the POU
RT   domain transcription factor pou3f1 (Oct-6, Tst-1, SCIP) in sciatic nerve.";
RL   J. Neurosci. 22:10217-10231(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION, TRANSPORTER ACTIVITY, AND TISSUE SPECIFICITY.
RX   PubMed=12809675; DOI=10.1016/s0888-7543(03)00099-5;
RA   Boll M., Foltz M., Rubio-Aliaga I., Daniel H.;
RT   "A cluster of proton/amino acid transporter genes in the human and mouse
RT   genomes.";
RL   Genomics 82:47-56(2003).
RN   [7]
RP   FUNCTION, AND TRANSPORTER ACTIVITY.
RX   PubMed=15291811; DOI=10.1111/j.1432-1033.2004.04268.x;
RA   Foltz M., Oechsler C., Boll M., Kottra G., Daniel H.;
RT   "Substrate specificity and transport mode of the proton-dependent amino
RT   acid transporter mPAT2.";
RL   Eur. J. Biochem. 271:3340-3347(2004).
RN   [8]
RP   FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=14600155; DOI=10.1074/jbc.m305556200;
RA   Rubio-Aliaga I., Boll M., Vogt Weisenhorn D.M., Foltz M., Kottra G.,
RA   Daniel H.;
RT   "The proton/amino acid cotransporter PAT2 is expressed in neurons with a
RT   different subcellular localization than its paralog PAT1.";
RL   J. Biol. Chem. 279:2754-2760(2004).
RN   [9]
RP   TISSUE SPECIFICITY.
RX   PubMed=15058382; DOI=10.1007/s00335-003-2319-3;
RA   Bermingham J.R. Jr., Pennington J.;
RT   "Organization and expression of the SLC36 cluster of amino acid transporter
RT   genes.";
RL   Mamm. Genome 15:114-125(2004).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Electrogenic proton/amino acid symporter with a high
CC       selectivity for the small side chains amino acids glycine, alanine and
CC       proline, where both L- and D-enantiomers are transported. Extension of
CC       the backbone length, as in beta-alanine and 4-aminobutanoate or
CC       methylation of the amino group, as in sarcosine and N,N-
CC       dimethylglycine, are also tolerated but decrease transport efficiency.
CC       A free carboxyl group is preferred. {ECO:0000269|PubMed:11959859,
CC       ECO:0000269|PubMed:12809675, ECO:0000269|PubMed:14600155,
CC       ECO:0000269|PubMed:15291811}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine(in) + H(+)(in) = glycine(out) + H(+)(out);
CC         Xref=Rhea:RHEA:28899, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305;
CC         Evidence={ECO:0000269|PubMed:11959859, ECO:0000269|PubMed:14600155,
CC         ECO:0000269|PubMed:15291811};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + L-alanine(in) = H(+)(out) + L-alanine(out);
CC         Xref=Rhea:RHEA:29443, ChEBI:CHEBI:15378, ChEBI:CHEBI:57972;
CC         Evidence={ECO:0000269|PubMed:11959859, ECO:0000269|PubMed:15291811};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-alanine(in) + H(+)(in) = D-alanine(out) + H(+)(out);
CC         Xref=Rhea:RHEA:28903, ChEBI:CHEBI:15378, ChEBI:CHEBI:57416;
CC         Evidence={ECO:0000269|PubMed:11959859, ECO:0000269|PubMed:15291811};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(out) + L-proline(out) = H(+)(in) + L-proline(in);
CC         Xref=Rhea:RHEA:28963, ChEBI:CHEBI:15378, ChEBI:CHEBI:60039;
CC         Evidence={ECO:0000269|PubMed:11959859, ECO:0000269|PubMed:12809675,
CC         ECO:0000269|PubMed:15291811};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-proline(out) + H(+)(out) = D-proline(in) + H(+)(in);
CC         Xref=Rhea:RHEA:70643, ChEBI:CHEBI:15378, ChEBI:CHEBI:57726;
CC         Evidence={ECO:0000269|PubMed:15291811};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-hydroxy-L-proline(in) + H(+)(in) = 4-hydroxy-L-proline(out)
CC         + H(+)(out); Xref=Rhea:RHEA:70663, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58419; Evidence={ECO:0000269|PubMed:15291811};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + L-serine(in) = H(+)(out) + L-serine(out);
CC         Xref=Rhea:RHEA:28887, ChEBI:CHEBI:15378, ChEBI:CHEBI:33384;
CC         Evidence={ECO:0000269|PubMed:11959859};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-serine(out) + H(+)(out) = D-serine(in) + H(+)(in);
CC         Xref=Rhea:RHEA:70647, ChEBI:CHEBI:15378, ChEBI:CHEBI:35247;
CC         Evidence={ECO:0000269|PubMed:11959859, ECO:0000269|PubMed:15291811};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-alanine(in) + H(+)(in) = beta-alanine(out) + H(+)(out);
CC         Xref=Rhea:RHEA:29459, ChEBI:CHEBI:15378, ChEBI:CHEBI:57966;
CC         Evidence={ECO:0000269|PubMed:11959859, ECO:0000269|PubMed:15291811};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-aminobutanoate(in) + H(+)(in) = 4-aminobutanoate(out) +
CC         H(+)(out); Xref=Rhea:RHEA:28915, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:59888; Evidence={ECO:0000269|PubMed:11959859,
CC         ECO:0000269|PubMed:15291811};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + sarcosine(in) = H(+)(out) + sarcosine(out);
CC         Xref=Rhea:RHEA:70655, ChEBI:CHEBI:15378, ChEBI:CHEBI:57433;
CC         Evidence={ECO:0000269|PubMed:15291811};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + N,N-dimethylglycine(in) = H(+)(out) + N,N-
CC         dimethylglycine(out); Xref=Rhea:RHEA:70659, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58251; Evidence={ECO:0000269|PubMed:15291811};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.59 mM for glycine {ECO:0000269|PubMed:11959859};
CC         KM=0.26 mM for L-alanine {ECO:0000269|PubMed:11959859};
CC         KM=0.12 mM for L-proline {ECO:0000269|PubMed:11959859};
CC         KM=43 mM for L-serine {ECO:0000269|PubMed:11959859};
CC         KM=6.5 mM for D-alanine {ECO:0000269|PubMed:11959859};
CC         KM=30.9 mM for 4-aminobutanoate/GABA {ECO:0000269|PubMed:11959859};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11959859,
CC       ECO:0000269|PubMed:14600155}; Multi-pass membrane protein
CC       {ECO:0000255}. Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:14600155}. Recycling endosome membrane
CC       {ECO:0000269|PubMed:14600155}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BHK3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BHK3-2; Sequence=VSP_032374, VSP_032375;
CC   -!- TISSUE SPECIFICITY: Expressed in spinal cord, brain, testis, lung,
CC       heart, colon, spleen, kidney and muscle. Found in neuronal cell bodies
CC       in the anterior horn, in spinal cord brain stem, cerebellum,
CC       hippocampus, hypothalamus, rhinencephalon, cerebral cortex, and
CC       olfactory bulb in the brain. Also expressed in bone and fat tissues.
CC       {ECO:0000269|PubMed:12809675, ECO:0000269|PubMed:14600155,
CC       ECO:0000269|PubMed:15058382}.
CC   -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AF453744; AAM80481.1; -; mRNA.
DR   EMBL; AF512429; AAM44854.1; -; mRNA.
DR   EMBL; AK041041; BAC30795.1; -; mRNA.
DR   EMBL; AK079053; BAC37515.1; -; mRNA.
DR   EMBL; AK086373; BAC39656.1; -; mRNA.
DR   EMBL; AK156409; BAE33702.1; -; mRNA.
DR   EMBL; AK160394; BAE35764.1; -; mRNA.
DR   EMBL; AL713870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC044800; AAH44800.1; -; mRNA.
DR   CCDS; CCDS24709.1; -. [Q8BHK3-1]
DR   RefSeq; NP_694810.2; NM_153170.3. [Q8BHK3-1]
DR   AlphaFoldDB; Q8BHK3; -.
DR   SMR; Q8BHK3; -.
DR   STRING; 10090.ENSMUSP00000045613; -.
DR   TCDB; 2.A.18.8.2; the amino acid/auxin permease (aaap) family.
DR   iPTMnet; Q8BHK3; -.
DR   PhosphoSitePlus; Q8BHK3; -.
DR   MaxQB; Q8BHK3; -.
DR   PaxDb; 10090-ENSMUSP00000045613; -.
DR   ProteomicsDB; 256565; -. [Q8BHK3-1]
DR   ProteomicsDB; 256566; -. [Q8BHK3-2]
DR   Antibodypedia; 28201; 141 antibodies from 25 providers.
DR   DNASU; 246049; -.
DR   Ensembl; ENSMUST00000039305.6; ENSMUSP00000045613.6; ENSMUSG00000020264.6. [Q8BHK3-1]
DR   GeneID; 246049; -.
DR   KEGG; mmu:246049; -.
DR   UCSC; uc007iyz.2; mouse. [Q8BHK3-1]
DR   UCSC; uc007iza.1; mouse. [Q8BHK3-2]
DR   AGR; MGI:1891430; -.
DR   CTD; 153201; -.
DR   MGI; MGI:1891430; Slc36a2.
DR   VEuPathDB; HostDB:ENSMUSG00000020264; -.
DR   eggNOG; KOG1304; Eukaryota.
DR   GeneTree; ENSGT00940000162044; -.
DR   HOGENOM; CLU_009646_0_2_1; -.
DR   InParanoid; Q8BHK3; -.
DR   OMA; SAMYVPN; -.
DR   OrthoDB; 3601817at2759; -.
DR   PhylomeDB; Q8BHK3; -.
DR   TreeFam; TF314873; -.
DR   Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR   Reactome; R-MMU-428559; Proton-coupled neutral amino acid transporters.
DR   SABIO-RK; Q8BHK3; -.
DR   BioGRID-ORCS; 246049; 1 hit in 76 CRISPR screens.
DR   PRO; PR:Q8BHK3; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q8BHK3; Protein.
DR   Bgee; ENSMUSG00000020264; Expressed in brown adipose tissue and 111 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR   GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR   GO; GO:0005280; F:amino acid:proton symporter activity; IDA:UniProtKB.
DR   GO; GO:0015187; F:glycine transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015180; F:L-alanine transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015193; F:L-proline transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0005297; F:proline:proton symporter activity; IDA:UniProtKB.
DR   GO; GO:0032973; P:amino acid export across plasma membrane; ISO:MGI.
DR   GO; GO:0015816; P:glycine transport; IDA:MGI.
DR   GO; GO:0015808; P:L-alanine transport; IDA:MGI.
DR   GO; GO:1900925; P:positive regulation of glycine import across plasma membrane; ISO:MGI.
DR   GO; GO:0035524; P:proline transmembrane transport; ISO:MGI.
DR   GO; GO:0015824; P:proline transport; IDA:MGI.
DR   GO; GO:1902600; P:proton transmembrane transport; IDA:MGI.
DR   GO; GO:0070881; P:regulation of proline transport; ISO:MGI.
DR   GO; GO:0010155; P:regulation of proton transport; ISO:MGI.
DR   InterPro; IPR013057; AA_transpt_TM.
DR   PANTHER; PTHR22950; AMINO ACID TRANSPORTER; 1.
DR   PANTHER; PTHR22950:SF185; PROTON-COUPLED AMINO ACID TRANSPORTER 2; 1.
DR   Pfam; PF01490; Aa_trans; 1.
DR   Genevisible; Q8BHK3; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Endoplasmic reticulum; Endosome;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..478
FT                   /note="Proton-coupled amino acid transporter 2"
FT                   /id="PRO_0000324820"
FT   TOPO_DOM        1..53
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        75..76
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        98..143
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        165..192
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        214..217
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        239..259
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        281..292
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        293..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        314..340
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        341..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        362..374
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        396..399
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        400..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        421..441
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        442..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        463..478
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         278..280
FT                   /note="LPL -> RFE (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_032374"
FT   VAR_SEQ         281..478
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_032375"
FT   CONFLICT        38
FT                   /note="S -> T (in Ref. 1; AAM80481 and 2; AAM44854)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        189
FT                   /note="V -> A (in Ref. 1; AAM80481 and 2; AAM44854)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   478 AA;  52063 MW;  0D4FE1C90F613A8A CRC64;
     MSVTKSARSP QVATPLNLDL PESAKKLQSQ DPSPANGSSS ESSKKTKGIT GFQTLVHLVK
     GNMGTGILGL PLAVKNAGIL MGPLSLLVMG LIACHCMHIL VRCAQRFCHR LNKPFMDYGD
     TVMHGLAFSP NAWLQNHAHW GRRVVSFFLI VTQLGFCCVY IVFLADNLKQ VVEAVNSTTI
     SCHKNETVVL TPTMDSRLYM LSFLPVLGLL VFVRNLRVLT IFSLLANISM LVSLVIIAQY
     IIQEIPDASQ LPLVASWKTY PLFFGTAIFS FESIGVVLPL ENKMKDARGF PTILSLGMSI
     ITTLYIAIGA LGYLRFGDDI KASITLNLPN CWLYQSVKLL YVVGILCTYA LQFYVPAEII
     IPLAVSQVSK RWALPVDLSI RLALVCLTCM LAILIPRLDL VLSLVGSVSS SALALIIPPL
     LEVVTYYGEG ISPLTVTKDA LISILGFMGF VVGTYQALDE LIKSGNSPAL SNSTMFIQ
//